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Conserved domains on  [gi|225446040|ref|XP_002270586|]
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(DL)-glycerol-3-phosphatase 2 [Vitis vinifera]

Protein Classification

HAD family hydrolase( domain architecture ID 10791471)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02811 PLN02811
hydrolase
 44-263 7.61e-168

hydrolase


:

Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 462.69  E-value: 7.61e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  44 MDGLLLDTEKFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVEETGISDSLSAEDFLVEREEMLRKLFPTSELM 123
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSDSLSPEDFLVEREAMLQDLFPTSDLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 124 PGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGEVFSLMHHVVLGDDPEVKQGKPSPDIFLAAARRFEGGPVDSQKI 203
Cdd:PLN02811  81 PGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRFEDGPVDPGKV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 204 LVFEDAPSGVGAAKNAGMYAVMVPDPRLDISFHEAADQVLSSLLDFNPNDWGLPPFPDTT 263
Cdd:PLN02811 161 LVFEDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPPFPDSS 220
 
Name Accession Description Interval E-value
PLN02811 PLN02811
hydrolase
 44-263 7.61e-168

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 462.69  E-value: 7.61e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  44 MDGLLLDTEKFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVEETGISDSLSAEDFLVEREEMLRKLFPTSELM 123
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSDSLSPEDFLVEREAMLQDLFPTSDLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 124 PGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGEVFSLMHHVVLGDDPEVKQGKPSPDIFLAAARRFEGGPVDSQKI 203
Cdd:PLN02811  81 PGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRFEDGPVDPGKV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 204 LVFEDAPSGVGAAKNAGMYAVMVPDPRLDISFHEAADQVLSSLLDFNPNDWGLPPFPDTT 263
Cdd:PLN02811 161 LVFEDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPPFPDSS 220
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 37-228 6.17e-107

subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and Gpp2; This subfamily includes Arabidopsis thaliana AtGpp1 and AtGpp2, and Drosophila GS1-like protein (Dmel\Gs1l) of unknown function. AtGpp1 and AtGpp2 are constitutively expressed in all the Arabidopsis tissues and unaffected under abiotic stress. Overexpression of AtGpp2 in transgenic Arabidopsis plants increases the specific DL-glycerol-3-phosphatase activity and improves the plants tolerance to salt, osmotic and oxidative stress. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319831 [Multi-domain]  Cd Length: 192  Bit Score: 307.35  E-value: 6.17e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  37 ISHVIFDMDGLLLDTEKFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVEETGISDSLSaEDFLVEREEMLRKL 116
Cdd:cd07529    1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLE-EEFDEQQEALAELF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 117 FPTSELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGEVFSLMHHVVLGDDPEVKQ-GKPSPDIFLAAARRFEG 195
Cdd:cd07529   80 MGTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVKGrGKPAPDIFLVAAKRFNE 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 225446040 196 GPVDSQKILVFEDAPSGVGAAKNAGMYAVMVPD 228
Cdd:cd07529  160 PPKDPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
37-249 2.37e-58

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 184.64  E-value: 2.37e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  37 ISHVIFDMDGLLLDTEKFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVEETGIsdSLSAEDFLVEREEMLRKL 116
Cdd:COG0637    2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGL--DLPEEELAARKEELYREL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 117 FPTSE--LMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGeVFSLMHHVVLGDDpeVKQGKPSPDIFLAAARRFE 194
Cdd:COG0637   80 LAEEGlpLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAG-LLDYFDVIVTGDD--VARGKPDPDIYLLAAERLG 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 225446040 195 ggpVDSQKILVFEDAPSGVGAAKNAGMYAVMVPDPRLDISFHEAADQVLSSLLDF 249
Cdd:COG0637  157 ---VDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 37-226 5.09e-29

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 108.20  E-value: 5.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040   37 ISHVIFDMDGLLLDTEKFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVEETGISDSLSAEDFLVERE-EMLRK 115
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSLEEIHQLAERKnELYRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  116 LFPT--SELMPGASRLVKHLHASGIPICVATGSHRRHFELKtqrHGEVFSLMHHVVLGDdpEVKQGKPSPDIFLAAARRF 193
Cdd:TIGR02009  81 LLRLtgVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILA---KLGLRDYFDAIVDAS--EVKNGKPHPETFLLAAELL 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 225446040  194 EggpVDSQKILVFEDAPSGVGAAKNAGMYAVMV 226
Cdd:TIGR02009 156 G---VPPNECIVFEDALAGVQAARAAGMFAVAV 185
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
40-226 3.93e-22

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 89.95  E-value: 3.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040   40 VIFDMDGLLLDTEKFYTEVQEIILARYNKTfDWSLK--AKMMGKKAIEAARVFVEETGISDSLsaeDFLVER--EEMLRK 115
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYG-ELSEEeiLKFIGLPLREIFRYLGVSEDEEEKI---EFYLRKynEELHDK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  116 LFptsELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGeVFSLMHHVVLGDDpeVKQGKPSPDIFLAAARRFEg 195
Cdd:pfam13419  77 LV---KPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLG-LEDYFDVIVGGDD--VEGKKPDPDPILKALEQLG- 149

                         170       180       190
                  ....*....|....*....|....*....|.
gi 225446040  196 gpVDSQKILVFEDAPSGVGAAKNAGMYAVMV 226
Cdd:pfam13419 150 --LKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
 
Name Accession Description Interval E-value
PLN02811 PLN02811
hydrolase
 44-263 7.61e-168

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 462.69  E-value: 7.61e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  44 MDGLLLDTEKFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVEETGISDSLSAEDFLVEREEMLRKLFPTSELM 123
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSDSLSPEDFLVEREAMLQDLFPTSDLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 124 PGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGEVFSLMHHVVLGDDPEVKQGKPSPDIFLAAARRFEGGPVDSQKI 203
Cdd:PLN02811  81 PGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRFEDGPVDPGKV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 204 LVFEDAPSGVGAAKNAGMYAVMVPDPRLDISFHEAADQVLSSLLDFNPNDWGLPPFPDTT 263
Cdd:PLN02811 161 LVFEDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPPFPDSS 220
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 37-228 6.17e-107

subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and Gpp2; This subfamily includes Arabidopsis thaliana AtGpp1 and AtGpp2, and Drosophila GS1-like protein (Dmel\Gs1l) of unknown function. AtGpp1 and AtGpp2 are constitutively expressed in all the Arabidopsis tissues and unaffected under abiotic stress. Overexpression of AtGpp2 in transgenic Arabidopsis plants increases the specific DL-glycerol-3-phosphatase activity and improves the plants tolerance to salt, osmotic and oxidative stress. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319831 [Multi-domain]  Cd Length: 192  Bit Score: 307.35  E-value: 6.17e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  37 ISHVIFDMDGLLLDTEKFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVEETGISDSLSaEDFLVEREEMLRKL 116
Cdd:cd07529    1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLE-EEFDEQQEALAELF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 117 FPTSELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGEVFSLMHHVVLGDDPEVKQ-GKPSPDIFLAAARRFEG 195
Cdd:cd07529   80 MGTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVKGrGKPAPDIFLVAAKRFNE 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 225446040 196 GPVDSQKILVFEDAPSGVGAAKNAGMYAVMVPD 228
Cdd:cd07529  160 PPKDPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
37-249 2.37e-58

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 184.64  E-value: 2.37e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  37 ISHVIFDMDGLLLDTEKFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVEETGIsdSLSAEDFLVEREEMLRKL 116
Cdd:COG0637    2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGL--DLPEEELAARKEELYREL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 117 FPTSE--LMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGeVFSLMHHVVLGDDpeVKQGKPSPDIFLAAARRFE 194
Cdd:COG0637   80 LAEEGlpLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAG-LLDYFDVIVTGDD--VARGKPDPDIYLLAAERLG 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 225446040 195 ggpVDSQKILVFEDAPSGVGAAKNAGMYAVMVPDPRLDISFHEAADQVLSSLLDF 249
Cdd:COG0637  157 ---VDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
PLN02940 PLN02940
riboflavin kinase
 34-261 2.61e-58

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 190.05  E-value: 2.61e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  34 KTSISHVIFDMDGLLLDTEKFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVEETGIsdSLSAEDFLVEREEML 113
Cdd:PLN02940   8 KKLVSHVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIVGKTPLEAAATVVEDYGL--PCSTDEFNSEITPLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 114 RKLFPTSELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRH---GEVFSlmhhVVLGDDpEVKQGKPSPDIFLAAA 190
Cdd:PLN02940  86 SEQWCNIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKISCHqgwKESFS----VIVGGD-EVEKGKPSPDIFLEAA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225446040 191 RRFEGGPVDSqkiLVFEDAPSGVGAAKNAGMYAVMVPD-PRLDISFhEAADQVLSSLLDFNPNDWGLPPFPD 261
Cdd:PLN02940 161 KRLNVEPSNC---LVIEDSLPGVMAGKAAGMEVIAVPSiPKQTHLY-SSADEVINSLLDLQPEKWGLPPFND 228
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 40-228 6.02e-39

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 132.74  E-value: 6.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  40 VIFDMDGLLLDTEKFYTEVqEIILARYNKTFDwslkakmmgkkaieaarvfveetgisdslsaedflvereEMLRKLFPt 119
Cdd:cd07505    2 VIFDMDGVLIDTEPLHRQA-WQLLERKNALLL---------------------------------------ELIASEGL- 40

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 120 sELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGEVFSLMHHVVLGDDpeVKQGKPSPDIFLAAARRFeggPVD 199
Cdd:cd07505   41 -KLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDD--VERGKPAPDIYLLAAERL---GVD 114

                        170       180
                 ....*....|....*....|....*....
gi 225446040 200 SQKILVFEDAPSGVGAAKNAGMYAVMVPD 228
Cdd:cd07505  115 PERCLVFEDSLAGIEAAKAAGMTVVAVPD 143
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 40-248 5.36e-32

uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized Bacillus subtilis YhcW; This subfamily includes the uncharacterized Bacillus subtilis YhcW. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 115.82  E-value: 5.36e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  40 VIFDMDGLLLDTEK-FYTEVQEIILARYNKTFdwslkakmmgkkaieaARVFVEETGIsdslsaedflvereemlrklfp 118
Cdd:cd16423    2 VIFDFDGVIVDTEPlWYEAWQELLNERRNELI----------------KRQFSEKTDL---------------------- 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 119 tsELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGeVFSLMHHVVLGDDpeVKQGKPSPDIFLAAARRFEggpV 198
Cdd:cd16423   44 --PPIEGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLG-LLDYFEVIVTGDD--VEKSKPDPDLYLEAAERLG---V 115

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 225446040 199 DSQKILVFEDAPSGVGAAKNAGMYAVMVPDPRLDISFHEAADQVLSSLLD 248
Cdd:cd16423  116 NPEECVVIEDSRNGVLAAKAAGMKCVGVPNPVTGSQDFSKADLVLSSFAE 165
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 37-226 5.09e-29

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 108.20  E-value: 5.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040   37 ISHVIFDMDGLLLDTEKFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVEETGISDSLSAEDFLVERE-EMLRK 115
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSLEEIHQLAERKnELYRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  116 LFPT--SELMPGASRLVKHLHASGIPICVATGSHRRHFELKtqrHGEVFSLMHHVVLGDdpEVKQGKPSPDIFLAAARRF 193
Cdd:TIGR02009  81 LLRLtgVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILA---KLGLRDYFDAIVDAS--EVKNGKPHPETFLLAAELL 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 225446040  194 EggpVDSQKILVFEDAPSGVGAAKNAGMYAVMV 226
Cdd:TIGR02009 156 G---VPPNECIVFEDALAGVQAARAAGMFAVAV 185
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 39-226 1.14e-26

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 102.11  E-value: 1.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040   39 HVIFDMDGLLLDTEKFYTEVQEiilARYNKTFDWSLKAKMMGKKAIEAARVFVEETGISDSLSAEDF----LVEREEMLR 114
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKLIN---REELGLVPDELGVSAVGRLELALRRFKAQYGRTISPEDAQLLykqlFYEQIEEEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  115 KLFPtselMPGASRLVKHLHASGIPICVATGSHRRHFelKTQRHGEVFSLMHHVVLGDDpeVKQGKPSPDIFLAAARRFe 194
Cdd:TIGR01509  78 KLKP----LPGVRALLEALRARGKKLALLTNSPRAHK--LVLALLGLRDLFDVVIDSSD--VGLGKPDPDIYLQALKAL- 148

                         170       180       190
                  ....*....|....*....|....*....|..
gi 225446040  195 ggPVDSQKILVFEDAPSGVGAAKNAGMYAVMV 226
Cdd:TIGR01509 149 --GLEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
37-249 1.30e-23

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 95.00  E-value: 1.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  37 ISHVIFDMDGLLLDTEKFYTEVQEIILARYN-KTFDWSLKAKMMGKKAIEAARVFVeetGISDSLSAEDFLVE-REEMLR 114
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGlPPLDLEELRALIGLGLRELLRRLL---GEDPDEELEELLARfRELYEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 115 KLFPTSELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGeVFSLMHHVVLGDDpeVKQGKPSPDIFLAAARRFE 194
Cdd:COG0546   78 ELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALG-LDDYFDAIVGGDD--VPPAKPKPEPLLEALERLG 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225446040 195 ggpVDSQKILVFEDAPSGVGAAKNAGMYAVMV------PDPRLDisfhEAADQVLSSLLDF 249
Cdd:COG0546  155 ---LDPEEVLMVGDSPHDIEAARAAGVPFIGVtwgygsAEELEA----AGADYVIDSLAEL 208
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 40-248 3.16e-22

subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p); This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319829 [Multi-domain]  Cd Length: 205  Bit Score: 90.87  E-value: 3.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  40 VIFDMDGLLLDTEKFYTEVQEIILARYNKTFDWSLKAkMMGKKAIEAARVFVEETGISDSLSAEdflvEREEMlRKLFPT 119
Cdd:cd07527    2 LLFDMDGTLVDSTPAVERAWHKWAKEHGVDPEEVLKV-SHGRRAIDVIRKLAPDDADIELVLAL----ETEEP-ESYPEG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 120 SELMPGASRLVKHLHASGIPICVATGSHRrhfELKTQRHgEVFSLMH--HVVLGDDpeVKQGKPSPDIFLAAARRfegGP 197
Cdd:cd07527   76 VIAIPGAVDLLASLPAAGDRWAIVTSGTR---ALAEARL-EAAGLPHpeVLVTADD--VKNGKPDPEPYLLGAKL---LG 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 225446040 198 VDSQKILVFEDAPSGVGAAKNAGMYAVMV-PDPRLDISFHEAADQVLSSLLD 248
Cdd:cd07527  147 LDPSDCVVFEDAPAGIKAGKAAGARVVAVnTSHDLEQLEAAGADLVVEDLSD 198
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
40-226 3.93e-22

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 89.95  E-value: 3.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040   40 VIFDMDGLLLDTEKFYTEVQEIILARYNKTfDWSLK--AKMMGKKAIEAARVFVEETGISDSLsaeDFLVER--EEMLRK 115
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYG-ELSEEeiLKFIGLPLREIFRYLGVSEDEEEKI---EFYLRKynEELHDK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  116 LFptsELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGeVFSLMHHVVLGDDpeVKQGKPSPDIFLAAARRFEg 195
Cdd:pfam13419  77 LV---KPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLG-LEDYFDVIVGGDD--VEGKKPDPDPILKALEQLG- 149

                         170       180       190
                  ....*....|....*....|....*....|.
gi 225446040  196 gpVDSQKILVFEDAPSGVGAAKNAGMYAVMV 226
Cdd:pfam13419 150 --LKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 37-220 4.30e-22

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 90.34  E-value: 4.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040   37 ISHVIFDMDGLLLDTEKFYTEVQEIILARYNKTF-------DWSLKAKMMGKKAIEAARVFVEETGISDSLSAEDFLVER 109
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKaivaaaeDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  110 EEMLRKLF------PTSELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGeVFSLMHHVVLGDDpeVKQGKPSP 183
Cdd:pfam00702  81 TVVLVELLgvialaDELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLG-LDDYFDVVISGDD--VGVGKPKP 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 225446040  184 DIFLAAARRFEggpVDSQKILVFEDAPSGVGAAKNAG 220
Cdd:pfam00702 158 EIYLAALERLG---VKPEEVLMVGDGVNDIPAAKAAG 191
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 40-226 4.28e-21

beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 87.36  E-value: 4.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040   40 VIFDMDGLLLDTEKFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVEETGisDSLSAEDF--LVERE-----EM 112
Cdd:TIGR01990   2 VIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGG--KKYSEEEKeeLAERKndyyvEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  113 LRKLFPTsELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQrhgEVFSLMHHVVlgDDPEVKQGKPSPDIFLAAArr 192
Cdd:TIGR01990  80 LKELTPA-DVLPGIKSLLADLKKNNIKIALASASKNAPTILEKL---ELIDYFDAIV--DPAELKKGKPDPEIFLAAA-- 151

                         170       180       190
                  ....*....|....*....|....*....|....
gi 225446040  193 fEGGPVDSQKILVFEDAPSGVGAAKNAGMYAVMV 226
Cdd:TIGR01990 152 -EGLGVSPSECIGIEDAQAGIEAIKAAGMFAVGV 184
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 37-249 2.37e-19

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 83.54  E-value: 2.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  37 ISHVIFDMDGLLLDTEKFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVEET--------GISDSLSAEDFLVE 108
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEYALWRRYERGEitfaellrRLLEELGLDLAEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 109 REEMLRKLFPTSELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGeVFSLMHHVVLGDdpEVKQGKPSPDIFLA 188
Cdd:COG1011   81 AEAFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLG-LDDLFDAVVSSE--EVGVRKPDPEIFEL 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225446040 189 AARRFeggPVDSQKILVFEDAPSG-VGAAKNAGMYAVMVPDPRLDISFHEAADQVLSSLLDF 249
Cdd:COG1011  158 ALERL---GVPPEEALFVGDSPETdVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAEL 216
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 40-249 9.31e-18

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319788 [Multi-domain]  Cd Length: 174  Bit Score: 78.49  E-value: 9.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  40 VIFDMDGLLLDTEKFYtevqeiiLARYNKTFDwslKAKMMGKKAieaaRVFVEetgisdslsaedflvereeMLRKLFPT 119
Cdd:cd02598    2 VIFDLDGVITDTAEYH-------YRAWKKLAD---KEELAARKN----RIYVE-------------------LIEELTPV 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 120 SELmPGASRLVKHLHASGIPICVAtgSHRRHFElKTQRHGEVFSLMHHVVlgDDPEVKQGKPSPDIFLAAARRFEggpVD 199
Cdd:cd02598   49 DVL-PGIASLLVDLKAKGIKIALA--SASKNAP-KILEKLGLAEYFDAIV--DGAVLAKGKPDPDIFLAAAEGLG---LN 119

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 225446040 200 SQKILVFEDAPSGVGAAKNAGMYAVMVPDPRLDIsfhEAADQVLSSLLDF 249
Cdd:cd02598  120 PKDCIGVEDAQAGIRAIKAAGFLVVGVGREEDLL---GADIVVPDTTADL 166
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 12-248 1.88e-16

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 77.06  E-value: 1.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  12 RNATPFRPPTLRFRAIAFSMAPKTSISHVIFDMDGLLLDTEKFytevqeiiLAR--YNKTF--------DWSLK-----A 76
Cdd:PLN02779  15 TRAGRRRRRRSRSTARVASASASALPEALLFDCDGVLVETERD--------GHRvaFNDAFkefglrpvEWDVElydelL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  77 KMMGKKaiEAARVFVEETG-----ISDSLSAEDflvEREEM-----LRK--LF------PTSELMPGASRLVKHLHASGI 138
Cdd:PLN02779  87 NIGGGK--ERMTWYFNENGwptstIEKAPKDEE---ERKELvdslhDRKteLFkeliesGALPLRPGVLRLMDEALAAGI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 139 PICVATGSHRRHFE--LKTQRHGEVFSLMHhVVLGDDpeVKQGKPSPDIFLAAARRFEggpVDSQKILVFEDAPSGVGAA 216
Cdd:PLN02779 162 KVAVCSTSNEKAVSkiVNTLLGPERAQGLD-VFAGDD--VPKKKPDPDIYNLAAETLG---VDPSRCVVVEDSVIGLQAA 235

                        250       260       270
                 ....*....|....*....|....*....|..
gi 225446040 217 KNAGMYAVMVPDPRLDISFHEAADQVLSSLLD 248
Cdd:PLN02779 236 KAAGMRCIVTKSSYTADEDFSGADAVFDCLGD 267
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
41-226 2.21e-16

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 75.11  E-value: 2.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  41 IFDMDGLLLDTEKFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVeETGISDsLSAEDFLVEREEMLRK-LFPT 119
Cdd:PRK10725   9 IFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAII-ELNQAD-LDPHALAREKTEAVKSmLLDS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 120 SELMPGASrLVKHLHASGiPICVATGSHRRHFElKTQRHGEVFSLMHHVVLGDDpeVKQGKPSPDIFLAAARRFEggpVD 199
Cdd:PRK10725  87 VEPLPLIE-VVKAWHGRR-PMAVGTGSESAIAE-ALLAHLGLRRYFDAVVAADD--VQHHKPAPDTFLRCAQLMG---VQ 158

                        170       180
                 ....*....|....*....|....*..
gi 225446040 200 SQKILVFEDAPSGVGAAKNAGMYAVMV 226
Cdd:PRK10725 159 PTQCVVFEDADFGIQAARAAGMDAVDV 185
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 40-221 3.81e-16

subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli 6-phosphogluconate phosphatase YieH; This subfamily includes Escherichia coli YieH/HAD3 an 6-phosphogluconate phosphatase, which can hydrolyzed purines and pyrimidines as secondary substrates. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate, and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319828 [Multi-domain]  Cd Length: 141  Bit Score: 73.12  E-value: 3.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  40 VIFDMDGLLLDTEkfytevqeiilarynktfdwslkakmmgkkaIEAARVFVEETGisdSLSAEDFlverEEMLRKLfpt 119
Cdd:cd07526    3 VIFDCDGVLVDSE-------------------------------VIAARVLVEVLA---ELGARVL----AAFEAEL--- 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 120 sELMPGASRLvkhLHASGIPICVATGSHRRHFELKTQRHGEVFSLMHHVVLGDDpeVKQGKPSPDIFLAAARRFEggpVD 199
Cdd:cd07526   42 -QPIPGAAAA---LSALTLPFCVASNSSRERLTHSLGLAGLLAYFEGRIFSASD--VGRGKPAPDLFLHAAAQMG---VA 112

                        170       180
                 ....*....|....*....|..
gi 225446040 200 SQKILVFEDAPSGVGAAKNAGM 221
Cdd:cd07526  113 PERCLVIEDSPTGVRAALAAGM 134
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 40-227 1.75e-13

subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides xylulose-1,5-bisphosphate phosphatase CbbY; This family includes Rhodobacter sphaeroides and Arabidopsis thaliana xylulose-1,5-bisphosphate phosphatase CbbY which convert xylulose-1,5-bisphosphate (a potent inhibitor of Ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco), to the non-inhibitory compound xylulose-5-phosphate. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319830 [Multi-domain]  Cd Length: 199  Bit Score: 67.40  E-value: 1.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  40 VIFDMDGLLLDTEK-----------------------FYTEVQEII-----LARYNKTFDWSLKAKMMGKKAIEA----- 86
Cdd:cd07528    2 LIFDVDGTLAETEElhrrafnnaffaergldwywdreLYGELLRVGggkerIAAYFEKVGWPESAPKDLKELIADlhkak 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  87 ARVFVEetgisdslsaedfLVEREEMlrklfptsELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRH--GEVFSL 164
Cdd:cd07528   82 TERYAE-------------LIAAGLL--------PLRPGVARLIDEAKAAGVRLAIATTTSPANVDALLSALlgPERRAI 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225446040 165 MHHVVLGDDpeVKQGKPSPDIFLAAARRFEggpVDSQKILVFEDAPSGVGAAKNAGMYAVMVP 227
Cdd:cd07528  141 FDAIAAGDD--VAEKKPDPDIYLLALERLG---VSPSDCLAIEDSAIGLQAAKAAGLPCIVTP 198
PRK11587 PRK11587
putative phosphatase; Provisional
 41-246 1.56e-11

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 62.32  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  41 IFDMDGLLLDT------------EKFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVE----ETGISDSLSAed 104
Cdd:PRK11587   7 LFDLDGTLVDSlpaverawsnwaDRHGIAPDEVLNFIHGKQAITSLRHFMAGASEAEIQAEFTRleqiEATDTEGITA-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 105 flvereemlrklfptselMPGASRLVKHLHASGIPICVAT-GS----HRRHfelktqRHGEVFSLMHHVVLgddPEVKQG 179
Cdd:PRK11587  85 ------------------LPGAIALLNHLNKLGIPWAIVTsGSvpvaSARH------KAAGLPAPEVFVTA---ERVKRG 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225446040 180 KPSPDIFLAAARRFEGGPvdsQKILVFEDAPSGVGAAKNAG--MYAVMVPD--PRLDisfheAADQVLSSL 246
Cdd:PRK11587 138 KPEPDAYLLGAQLLGLAP---QECVVVEDAPAGVLSGLAAGchVIAVNAPAdtPRLD-----EVDLVLHSL 200
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 37-229 7.29e-11

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 60.05  E-value: 7.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  37 ISHVIFDMDGLLLD------TEKFYTEVQEIILARYNKTFDWSLKAKMM-GKK-AIEAARVFVEETGISDslSAEDFlve 108
Cdd:cd02603    1 IRAVLFDFGGVLIDpdpaaaVARFEALTGEPSEFVLDTEGLAGAFLELErGRItEEEFWEELREELGRPL--SAELF--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 109 rEEMLRKLFptsELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGEVFSLMHHVVLGDDpeVKQGKPSPDIFLA 188
Cdd:cd02603   76 -EELVLAAV---DPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLFDGVVESCR--LGVRKPDPEIYQL 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 225446040 189 AARRFEggpVDSQKILVFEDAPSGVGAAKNAGMYAVMVPDP 229
Cdd:cd02603  150 ALERLG---VKPEEVLFIDDREENVEAARALGIHAILVTDA 187
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 72-253 1.00e-09

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 57.73  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  72 WSLKAKMMGKK-----AIEAARVFVEETGISDSLS-AEDFL------VEREEMLRKL-FPTSELMPGASRLVKHLHASGI 138
Cdd:PLN03243  47 WRALAEEEGKRpppafLLKRAEGMKNEQAISEVLCwSRDFLqmkrlaIRKEDLYEYMqGGLYRLRPGSREFVQALKKHEI 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 139 PICVATGSHRRHFELKTQRHGeVFSLMHHVVLGDDpeVKQGKPSPDIFLAAARRFEGGPvdsQKILVFEDAPSGVGAAKN 218
Cdd:PLN03243 127 PIAVASTRPRRYLERAIEAVG-MEGFFSVVLAAED--VYRGKPDPEMFMYAAERLGFIP---ERCIVFGNSNSSVEAAHD 200

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 225446040 219 AGMYAVMVP--DPRLDISfheAADQVLSSLLDFNPND 253
Cdd:PLN03243 201 GCMKCVAVAgkHPVYELS---AGDLVVRRLDDLSVVD 234
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 39-220 1.88e-09

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 55.48  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040   39 HVIFDMDGLLLDtekfYTEVQEIILARYNKTFDWSLKAkmmgKKAIEAARVFVEEtgISDSLSAEDFLVEREEMLRKLFP 118
Cdd:TIGR01549   1 AILFDIDGTLVD----IKFAIRRAFPQTFEEFGLDPAS----FKALKQAGGLAEE--EWYRIATSALEELQGRFWSEYDA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  119 TSELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGeVFSLMHHVVLGDDPevkQGKPSPDIFLAAARRFEGGPv 198
Cdd:TIGR01549  71 EEAYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFG-LGDYFELILVSDEP---GSKPEPEIFLAALESLGVPP- 145

                         170       180
                  ....*....|....*....|..
gi 225446040  199 dsqKILVFEDAPSGVGAAKNAG 220
Cdd:TIGR01549 146 ---EVLHVGDNLNDIEGARNAG 164
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 1-226 1.15e-08

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 55.63  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040    1 MLGIRIPIGVWRNATPFRPPTLRFRAIAFSMAPKTS------ISHVIFDMDGLLLDTEKFYTEVQEIILAR--YNKT--- 69
Cdd:PLN02919   33 IRGRRSRSGVWLGKNGGARSKSCAKVEEKSRGAEIAteewgkVSAVLFDMDGVLCNSEEPSRRAAVDVFAEmgVEVTved 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040   70 ---FDWSLKAKMMGkkaieaarvfveetGISDSLSAEDFlvEREEMLRKLF---------PTSEL-MPGASRLVKHLHAS 136
Cdd:PLN02919  113 fvpFMGTGEANFLG--------------GVASVKGVKGF--DPDAAKKRFFeiylekyakPNSGIgFPGALELITQCKNK 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  137 GIPICVATGSHRRHFELKTQRHGEVFSLMHHVVLGDDPEvkQGKPSPDIFLAAARRFEggpVDSQKILVFEDAPSGVGAA 216
Cdd:PLN02919  177 GLKVAVASSADRIKVDANLAAAGLPLSMFDAIVSADAFE--NLKPAPDIFLAAAKILG---VPTSECVVIEDALAGVQAA 251

                         250
                  ....*....|
gi 225446040  217 KNAGMYAVMV 226
Cdd:PLN02919  252 RAAGMRCIAV 261
HAD pfam12710
haloacid dehalogenase-like hydrolase;
40-217 1.79e-08

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 52.92  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040   40 VIFDMDGLLLDTE------KFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVEETgisDSLSAEDFLVEREEML 113
Cdd:pfam12710   1 ALFDLDGTLLDGDslflliRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGARELLRAL---LAGLPEEDAAELERFV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  114 RKLFpTSELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGevfslmHHVVLGDDPEVKQGKPSPDIF------- 186
Cdd:pfam12710  78 AEVA-LPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELG------FDEVLATELEVDDGRFTGELRligppca 150

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 225446040  187 -------LAAARRFEGGPVDSQKILVFEDAPSGVGAAK 217
Cdd:pfam12710 151 gegkvrrLRAWLAARGLGLDLADSVAYGDSPSDLPMLR 188
PRK10826 PRK10826
hexitol phosphatase HxpB;
31-251 2.27e-08

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 53.03  E-value: 2.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  31 MAPKTSISHVIFDMDGLLLDTEKFYTEVQEIILA------------------RYNKTFD-WSLKAKMMGKKAIEAARVFV 91
Cdd:PRK10826   1 MSTPRQILAAIFDMDGLLIDSEPLWDRAELDVMAslgvdisrreelpdtlglRIDQVVDlWYARQPWNGPSRQEVVQRII 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  92 EETgISdslsaedfLVEReemlrklfpTSELMPGASRLVKHLHASGIPICVATGShrrhfelktqrhgevFSLMHHVVLG 171
Cdd:PRK10826  81 ARV-IS--------LIEE---------TRPLLPGVREALALCKAQGLKIGLASAS---------------PLHMLEAVLT 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 172 -----DDPEVKQ-------GKPSPDIFLAAARRFEggpVDSQKILVFEDAPSGVGAAKNAGMYAVMVPDPRLdisFHEA- 238
Cdd:PRK10826 128 mfdlrDYFDALAsaeklpySKPHPEVYLNCAAKLG---VDPLTCVALEDSFNGMIAAKAARMRSIVVPAPEQ---QNDPr 201

                        250
                 ....*....|....*.
gi 225446040 239 ---ADQVLSSLLDFNP 251
Cdd:PRK10826 202 walADVKLESLTELTA 217
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 40-226 1.49e-07

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 50.47  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  40 VIFDMDGLLLDTEKFYTEVQEIILARYNKTFDWSLKAK-MMGKKAIEAARVFVEETGISDSLSAEDFLvEREEMLRKLF- 117
Cdd:cd07533    2 VIFDWDGTLADSQHNIVAAMTAAFADLGLPVPSAAEVRsIIGLSLDEAIARLLPMATPALVAVAERYK-EAFDILRLLPe 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 118 PTSELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGevfsLMHHVVL----GDDPevkqGKPSPDIFLAAARrf 193
Cdd:cd07533   81 HAEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHG----LGGYFDAtrtaDDTP----SKPHPEMLREILA-- 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 225446040 194 EGGpVDSQKILVFEDAPSGVGAAKNAGMYAVMV 226
Cdd:cd07533  151 ELG-VDPSRAVMVGDTAYDMQMAANAGAHAVGV 182
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 29-224 6.03e-07

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 49.07  E-value: 6.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  29 FSMAPKTSISHVIFDMDGLLLDTEKF-YTEVQEIILA-RYNKTFDWSLK---AKMMGKKAIEAARVFVEEtgisDSLSAE 103
Cdd:PLN02770  14 SSLSGLAPLEAVLFDVDGTLCDSDPLhYYAFREMLQEiNFNGGVPITEEffvENIAGKHNEDIALGLFPD----DLERGL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 104 DFLVEREEMLRKLFPtSELMP--GASRLVKHLHASGIPICVATGSHRRHFELKTQRHGeVFSLMHHVVLGDdpEVKQGKP 181
Cdd:PLN02770  90 KFTDDKEALFRKLAS-EQLKPlnGLYKLKKWIEDRGLKRAAVTNAPRENAELMISLLG-LSDFFQAVIIGS--ECEHAKP 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 225446040 182 SPDIFLAAarrFEGGPVDSQKILVFEDAPSGVGAAKNAGMYAV 224
Cdd:PLN02770 166 HPDPYLKA---LEVLKVSKDHTFVFEDSVSGIKAGVAAGMPVV 205
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
40-227 1.12e-06

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 48.27  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  40 VIFDMDGLLLDTekfyteVQEIILArynktFDWSLKAkmMGKKAIEA----------ARVFVEE--TGISDSLSAEDFlv 107
Cdd:PRK13222   9 VAFDLDGTLVDS------APDLAAA-----VNAALAA--LGLPPAGEervrtwvgngADVLVERalTWAGREPDEELL-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 108 ereEMLRKLFPT---------SELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHG--EVFSLmhhVVLGDDpeV 176
Cdd:PRK13222  74 ---EKLRELFDRhyaenvaggSRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGiaDYFSV---VIGGDS--L 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 225446040 177 KQGKPSPDIFLAAARRFEGGPvdsQKILVFEDAPSGVGAAKNAGMYAVMVP 227
Cdd:PRK13222 146 PNKKPDPAPLLLACEKLGLDP---EEMLFVGDSRNDIQAARAAGCPSVGVT 193
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 40-248 1.88e-06

Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGP; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 47.23  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  40 VIFDMDGLLLDTekfyteVQEIILArynktFDWSLKAkmMGKKAIEAARV--FVE-------ETGISDSLSAEDFLVERE 110
Cdd:cd16417    2 VAFDLDGTLVDS------APDLAEA-----ANAMLAA--LGLPPLPEETVrtWIGngadvlvERALTGAREAEPDEELFK 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 111 EmLRKLF---------PTSELMPGASRLVKHLHASGIPICVATGSHRRH-FELKTQrHG--EVFSLmhhVVLGDDpeVKQ 178
Cdd:cd16417   69 E-ARALFdrhyaetlsVHSHLYPGVKEGLAALKAQGYPLACVTNKPERFvAPLLEA-LGisDYFSL---VLGGDS--LPE 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225446040 179 GKPSPDIFLAAARRFEggpVDSQKILVFEDAPSGVGAAKNAGMYAVMVP----DPRlDISfHEAADQVLSSLLD 248
Cdd:cd16417  142 KKPDPAPLLHACEKLG---IAPAQMLMVGDSRNDILAARAAGCPSVGLTygynYGE-DIA-ASGPDAVIDSLAE 210
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 126-226 3.23e-06

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 44.69  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 126 ASRLVKHLHASGIPICVATGSHRRHFElKTQRHGEVFSLMHHVVLGDDpeVKQGKPSPDIFLAAARRFeggPVDSQKILV 205
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALR-ALLEKLGLGDLFDGIIGSDG--GGTPKPKPKPLLLLLLKL---GVDPEEVLF 85

                         90       100
                 ....*....|....*....|.
gi 225446040 206 FEDAPSGVGAAKNAGMYAVMV 226
Cdd:cd01427   86 VGDSENDIEAARAAGGRTVAV 106
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 35-221 5.17e-06

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 46.23  E-value: 5.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  35 TSISHVIFDMDGLLLDTEKFYTEVQEIILARYNKTFDWS-LKAKMMGKKAIEAARVFVEETGIsdSLSAEDF-LVEREEM 112
Cdd:PRK10563   2 SQIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEeVFKRFKGVKLYEIIDIISKEHGV--TLAKAELePVYRAEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 113 LRkLFPTS-ELMPGASRLVKHLHasgIPICVATG---SHRRHFELKTQrhgevfsLMHHV--VLGDDPEVKQGKPSPDIF 186
Cdd:PRK10563  80 AR-LFDSElEPIAGANALLESIT---VPMCVVSNgpvSKMQHSLGKTG-------MLHYFpdKLFSGYDIQRWKPDPALM 148

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 225446040 187 LAAARRFEggpVDSQKILVFEDAPSGVGAAKNAGM 221
Cdd:PRK10563 149 FHAAEAMN---VNVENCILVDDSSAGAQSGIAAGM 180
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 41-225 7.42e-06

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases


Pssm-ID: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 45.06  E-value: 7.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  41 IFDMDGLLLDTEKFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVEETgisdslsaEDFLVEREEMLRKLFPTS 120
Cdd:cd07523    3 IWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIIKESSVQFAIQYYAEV--------PDLEEEYKELEAEYLAKP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 121 ELMPGASRLVKHLHASGIPICVATgsHRRHFELKTQRHGEVFSLMHHVVLGDDPEVKqgKPSPDIFLAAARRFEggpVDS 200
Cdd:cd07523   75 ILFPGAKAVLRWIKEQGGKNFLMT--HRDHSALTILKKDGIASYFTEIVTSDNGFPR--KPNPEAINYLLNKYQ---LNP 147

                        170       180
                 ....*....|....*....|....*
gi 225446040 201 QKILVFEDAPSGVGAAKNAGMYAVM 225
Cdd:cd07523  148 EETVMIGDRELDIEAGHNAGISTIL 172
Hydrolase_like pfam13242
HAD-hyrolase-like;
179-248 1.73e-05

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 41.83  E-value: 1.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225446040  179 GKPSPDIFLAAARRFEggpVDSQKILVFEDAP-SGVGAAKNAGMYAVMVP----DPRLDISFHEAADQVLSSLLD 248
Cdd:pfam13242   3 GKPNPGMLERALARLG---LDPERTVMIGDRLdTDILGAREAGARTILVLtgvtRPADLEKAPIRPDYVVDDLAE 74
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 179-243 7.00e-05

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 43.04  E-value: 7.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 179 GKPSPDIFLAAARRFEGGPvdSQKILVFEDAPSGVGAAKNAGMYAVMV----------------PDPRLDiSFHEAADQV 242
Cdd:cd07509  171 GKPSPEFFLSALRSLGVDP--EEAVMIGDDLRDDVGGAQACGMRGILVrtgkyrpsdekkpnvpPDLTAD-SFADAVDHI 247


                 .
gi 225446040 243 L 243
Cdd:cd07509  248 L 248
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 37-226 9.79e-05

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 42.27  E-value: 9.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  37 ISHVIFDMDGLLLDTekfyteVQEIIlarynKTFDWSLKAKMMGKKAIEAARVFVEEtGISDSLSA--EDFLVEREEMLR 114
Cdd:cd02616    1 ITTILFDLDGTLIDT------NELII-----KSFNHTLKEYGLEGYTREEVLPFIGP-PLRETFEKidPDKLEDMVEEFR 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 115 KLF-----PTSELMPGASRLVKHLHASGIPICVATgSHRRHFELKTQRHGEVFSLMHHVVLGDDpeVKQGKPSPDIFLAA 189
Cdd:cd02616   69 KYYrehndDLTKEYPGVYETLARLKSQGIKLGVVT-TKLRETALKGLKLLGLDKYFDVIVGGDD--VTHHKPDPEPVLKA 145

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 225446040 190 ARRFEGGPvdsQKILVFEDAPSGVGAAKNAGMYAVMV 226
Cdd:cd02616  146 LELLGAEP---EEALMVGDSPHDILAGKNAGVKTVGV 179
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 40-185 1.10e-04

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 42.13  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  40 VIFDMDGLLLDTE------KFYTEVQEIILARYNKTFDWSLKAKMMGKKAIEAARVFVeeTGISDSLSAEDFLVEREEML 113
Cdd:COG0560    6 AVFDLDGTLIAGEsidelaRFLGRRGLVDRREVLEEVAAITERAMAGELDFEESLRFR--VALLAGLPEEELEELAERLF 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225446040 114 RKLFPtseLMPGASRLVKHLHASGIPICVATGShrrhFELKTQRHGEVFSLMHhvVLGDDPEVKQGKPSPDI 185
Cdd:COG0560   84 EEVPR---LYPGARELIAEHRAAGHKVAIVSGG----FTFFVEPIAERLGIDH--VIANELEVEDGRLTGEV 146
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 120-228 1.36e-03

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 38.15  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040  120 SELMPGASRLVKHLHASGIPICVAT---GSHRRHFELKTQRHGEVFSL---MHHVVLGDDPEVKqgKPSPDIFLAAARRF 193
Cdd:TIGR01662  24 RILYPEVPDALAELKEAGYKVVIVTnqsGIGRGYFSRSFSGRVARRLEelgVPIDILYACPGCR--KPKPGMFLEALKRF 101

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 225446040  194 EGgpVDSQKILVFEDAP-SGVGAAKNAGMYAVMVPD 228
Cdd:TIGR01662 102 NE--IDPEESVYVGDQDlTDLQAAKRVGLATILVAP 135
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
 112-226 2.78e-03

Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; Degradation of the ubiquitous natural phosphonate 2-aminoethylphosphonate (AEP) into useable forms of nitrogen, carbon, and phosphorus is a two-step metabolic pathway. The first step, catalyzed by AEP transaminase, involves the transfer of NH3 from AEP to pyruvate, yielding phosphonoacetaldehyde (P-Ald) and alanine. In the second step, phosphonatase catalyzes the hydrolytic P-C bond cleavage of P-Ald to form orthophosphate and acetaldehyde. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319785 [Multi-domain]  Cd Length: 242  Bit Score: 38.05  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 112 MLRKLFPTSELMPGASRLVKHLHASGIPICVATGSHRRHFELKTQRHGEVFSLMHHVVLGDDpeVKQGKPSPDIFLAAAR 191
Cdd:cd02586   89 LIASLAEYSSPIPGVLEVIAKLRARGIKIGSTTGYTREMMDIVLPEAAAQGYRPDSLVTPDD--VPAGRPYPWMCYKNAI 166

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 225446040 192 RFEGGPVDSQ-KIlvfEDAPSGVGAAKNAGMYAVMV 226
Cdd:cd02586  167 ELGVYDVAAVvKV---GDTVPDIKEGLNAGMWTVGV 199
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 122-224 7.83e-03

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 35.21  E-value: 7.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225446040 122 LMPGASRLVKHLHAsGIPICVATGSHRRHFELKTQRHGeVFSLMHHVVLGDdpEVKQGKPSPDIFLAAARRFEGGPVDSq 201
Cdd:cd04305   10 LLPGAKELLEELKK-GYKLGIITNGPTEVQWEKLEQLG-IHKYFDHIVISE--EVGVQKPNPEIFDYALNQLGVKPEET- 84

                         90       100
                 ....*....|....*....|...
gi 225446040 202 kILVFEDAPSGVGAAKNAGMYAV 224
Cdd:cd04305   85 -LMVGDSLESDILGAKNAGIKTV 106
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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